메뉴 건너뛰기




Volumn 74, Issue 11, 2006, Pages 6124-6134

Protease activity, secretion, cell entry, cytotoxicity, and cellular targets of secreted autotransporter toxin of uropathogenic Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI ENTEROTOXIN; FODRIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LIM DOMAIN ONLY PROTEIN 7; LIM PROTEIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MICROTUBULE ASSOCIATED PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN SPATE; PROTEINASE; RAP GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; SECRETED AUTOTRANSPORTER TOXIN; SERINE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 33750475609     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.01086-06     Document Type: Article
Times cited : (53)

References (55)
  • 2
    • 0034237676 scopus 로고    scopus 로고
    • Spindle assembly and the art of regulating microtubule dynamics by MAPs and Stathmin/Op18
    • Andersen, S. S. 2000. Spindle assembly and the art of regulating microtubule dynamics by MAPs and Stathmin/Op18. Trends Cell Biol. 10:261-267.
    • (2000) Trends Cell Biol. , vol.10 , pp. 261-267
    • Andersen, S.S.1
  • 3
    • 0036039736 scopus 로고    scopus 로고
    • Type 1 fimbriae and extracellular polysaccharides are preeminent uropathogenic Escherichia coli virulence determinants in the murine urinary tract
    • Bahrani-Mougeot, F. K., E. L. Buckles, C. V. Lockatell, J. R. Hebel, D. E. Johnson, C. M. Tang, and M. S. Donnenberg. 2002. Type 1 fimbriae and extracellular polysaccharides are preeminent uropathogenic Escherichia coli virulence determinants in the murine urinary tract. Mol. Microbiol. 45:1079-1093.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1079-1093
    • Bahrani-Mougeot, F.K.1    Buckles, E.L.2    Lockatell, C.V.3    Hebel, J.R.4    Johnson, D.E.5    Tang, C.M.6    Donnenberg, M.S.7
  • 4
    • 0037623278 scopus 로고    scopus 로고
    • Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservation
    • Baines, A. J. 2003. Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservation. Cell. Mol. Biol. Lett. 8:195-214.
    • (2003) Cell. Mol. Biol. Lett. , vol.8 , pp. 195-214
    • Baines, A.J.1
  • 5
    • 0029905387 scopus 로고    scopus 로고
    • The spectrin-based membrane skeleton as a membrane protein-sorting machine
    • Beck, K. A., and W. J. Nelson. 1996. The spectrin-based membrane skeleton as a membrane protein-sorting machine. Am. J. Physiol. 270:C1263-C1270.
    • (1996) Am. J. Physiol. , vol.270
    • Beck, K.A.1    Nelson, W.J.2
  • 6
    • 0029166295 scopus 로고
    • SepA, the major extracellular protein of Shigella flexneri: Autonomous secretion and involvement in tissue invasion
    • Benjelloun-Touimi, Z., P. J. Sansonetti, and C. Parsot. 1995. SepA, the major extracellular protein of Shigella flexneri: autonomous secretion and involvement in tissue invasion. Mol. Microbiol. 17:123-135.
    • (1995) Mol. Microbiol. , vol.17 , pp. 123-135
    • Benjelloun-Touimi, Z.1    Sansonetti, P.J.2    Parsot, C.3
  • 7
    • 3543013141 scopus 로고    scopus 로고
    • SepA, the 110 kDa protein secreted by Shigella flexneri: Two-domain structure and proteolytic activity
    • Benjelloun-Touimi, Z., M. Si Tahar, C. Montecucco, P. J. Sansonetti, and C. Parsot. 1998. SepA, the 110 kDa protein secreted by Shigella flexneri: two-domain structure and proteolytic activity. Microbiology 144:1815-1822.
    • (1998) Microbiology , vol.144 , pp. 1815-1822
    • Benjelloun-Touimi, Z.1    Si Tahar, M.2    Montecucco, C.3    Sansonetti, P.J.4    Parsot, C.5
  • 8
    • 0037451803 scopus 로고    scopus 로고
    • GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila
    • Bernards, A. 2003. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim. Biophys. Acta 1603:47-82.
    • (2003) Biochim. Biophys. Acta , vol.1603 , pp. 47-82
    • Bernards, A.1
  • 9
    • 0030917724 scopus 로고    scopus 로고
    • EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7, cleaves human coagulation factor V
    • Brunder, W., H. Schmidt, and H. Karch. 1997. EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7, cleaves human coagulation factor V. Mol. Microbiol. 24:767-778.
    • (1997) Mol. Microbiol. , vol.24 , pp. 767-778
    • Brunder, W.1    Schmidt, H.2    Karch, H.3
  • 11
    • 18544381071 scopus 로고    scopus 로고
    • Introduction to poly(ADP-ribose) metabolism
    • Diefenbach, J., and A. Burkle. 2005. Introduction to poly(ADP-ribose) metabolism. Cell. Mol. Life Sci. 62:721-730.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 721-730
    • Diefenbach, J.1    Burkle, A.2
  • 12
    • 0036893427 scopus 로고    scopus 로고
    • Functional comparison of serine protease autotransporters of Enterobacteriaceae
    • Dutta, P. R., R. Cappello, F. Navarro-Garcia, and J. P. Nataro. 2002. Functional comparison of serine protease autotransporters of Enterobacteriaceae. Infect. Immun. 70:7105-7113.
    • (2002) Infect. Immun. , vol.70 , pp. 7105-7113
    • Dutta, P.R.1    Cappello, R.2    Navarro-Garcia, F.3    Nataro, J.P.4
  • 14
    • 0029021466 scopus 로고
    • Bacterial virulence characteristics of Escherichia coli isolates from first-time urinary tract infection
    • Foxman, B., L. Zhang, K. Palin, P. Tallman, and C. F. Marrs. 1995. Bacterial virulence characteristics of Escherichia coli isolates from first-time urinary tract infection. J. Infect. Dis. 171:1514-1521.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1514-1521
    • Foxman, B.1    Zhang, L.2    Palin, K.3    Tallman, P.4    Marrs, C.F.5
  • 15
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and E. Ruoslahti. 1999. Integrin signaling. Science 285:1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 16
    • 0033810425 scopus 로고    scopus 로고
    • Identification of sat, an autotransporter toxin produced by uropathogenic Escherichia coli
    • Guyer, D. M., I. R. Henderson, J. P. Nataro, and H. L. Mobley. 2000. Identification of sat, an autotransporter toxin produced by uropathogenic Escherichia coli. Mol. Microbiol. 38:53-66.
    • (2000) Mol. Microbiol. , vol.38 , pp. 53-66
    • Guyer, D.M.1    Henderson, I.R.2    Nataro, J.P.3    Mobley, H.L.4
  • 17
    • 0036070744 scopus 로고    scopus 로고
    • Sat, the secreted autotransporter toxin of uropathogenic Escherichia coli, is a vacuolating cytotoxin for bladder and kidney epithelial cells
    • Guyer, D. M., S. Radulovic, F. E. Jones, and H. L. Mobley. 2002. Sat, the secreted autotransporter toxin of uropathogenic Escherichia coli, is a vacuolating cytotoxin for bladder and kidney epithelial cells. Infect. Immun. 70:4539-4546.
    • (2002) Infect. Immun. , vol.70 , pp. 4539-4546
    • Guyer, D.M.1    Radulovic, S.2    Jones, F.E.3    Mobley, H.L.4
  • 18
    • 0030901705 scopus 로고    scopus 로고
    • Pathogenicity islands of virulent bacteria: Structure, function and impact on microbial evolution
    • Hacker, J., G. Blum-Oehler, I. Muhldorfer, and H. Tschape. 1997. Pathogenicity islands of virulent bacteria: structure, function and impact on microbial evolution. Mol. Microbiol. 23:1089-1097.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1089-1097
    • Hacker, J.1    Blum-Oehler, G.2    Muhldorfer, I.3    Tschape, H.4
  • 19
    • 0348141893 scopus 로고    scopus 로고
    • Autotransporter genes pic and tsh are associated with Escherichia coli strains that cause acute pyelonephritis and are expressed during urinary tract infection
    • Heimer, S. R., D. A. Rasko, C. V. Lockatell, D. E. Johnson, and H. L. Mobley. 2004. Autotransporter genes pic and tsh are associated with Escherichia coli strains that cause acute pyelonephritis and are expressed during urinary tract infection. Infect. Immun. 72:593-597.
    • (2004) Infect. Immun. , vol.72 , pp. 593-597
    • Heimer, S.R.1    Rasko, D.A.2    Lockatell, C.V.3    Johnson, D.E.4    Mobley, H.L.5
  • 20
    • 0034541135 scopus 로고    scopus 로고
    • Autotransporter proteins, evolution and redefining protein secretion
    • Henderson, I. R., R. Cappello, and J. P. Nataro. 2000. Autotransporter proteins, evolution and redefining protein secretion. Trends Microbiol. 8:529-532.
    • (2000) Trends Microbiol. , vol.8 , pp. 529-532
    • Henderson, I.R.1    Cappello, R.2    Nataro, J.P.3
  • 21
    • 0032734808 scopus 로고    scopus 로고
    • Characterization of Pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli
    • Henderson, I. R., J. Czeczulin, C. Eslava, F. Noriega, and J. P. Nataro. 1999. Characterization of Pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli. Infect. Immun. 67:5587-5596.
    • (1999) Infect. Immun. , vol.67 , pp. 5587-5596
    • Henderson, I.R.1    Czeczulin, J.2    Eslava, C.3    Noriega, F.4    Nataro, J.P.5
  • 22
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson, I. R., and J. P. Nataro. 2001. Virulence functions of autotransporter proteins. Infect. Immun. 69:1231-1243.
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 23
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: Structure and function of the autotransporter proteins
    • Henderson, I. R., F. Navarro-Garcia, and J. P. Nataro. 1998. The great escape: structure and function of the autotransporter proteins. Trends Microbiol. 6:370-378.
    • (1998) Trends Microbiol. , vol.6 , pp. 370-378
    • Henderson, I.R.1    Navarro-Garcia, F.2    Nataro, J.P.3
  • 24
    • 0030693901 scopus 로고    scopus 로고
    • Structural determinants of processing and secretion of the Haemophilus influenzae hap protein
    • Hendrixson, D. R., M. L. de la Morena, C. Stathopoulos, and J. W. St. Geme III. 1997. Structural determinants of processing and secretion of the Haemophilus influenzae hap protein. Mol. Microbiol. 26:505-518.
    • (1997) Mol. Microbiol. , vol.26 , pp. 505-518
    • Hendrixson, D.R.1    De La Morena, M.L.2    Stathopoulos, C.3    St. Geme III, J.W.4
  • 25
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 26
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 27
    • 0026060005 scopus 로고
    • Virulence factors in Escherichia coli urinary tract infection
    • Johnson, J. R. 1991. Virulence factors in Escherichia coli urinary tract infection. Clin. Microbiol. Rev. 4:80-128.
    • (1991) Clin. Microbiol. Rev. , vol.4 , pp. 80-128
    • Johnson, J.R.1
  • 28
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • Kadrmas, J. L., and M. C. Beckerle. 2004. The LIM domain: from the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell Biol. 5:920-931.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 29
    • 4644274735 scopus 로고    scopus 로고
    • Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain
    • Kostakioti, M., and C. Stathopoulos. 2004. Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain. Infect. Immun. 72:5548-5554.
    • (2004) Infect. Immun. , vol.72 , pp. 5548-5554
    • Kostakioti, M.1    Stathopoulos, C.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0030688998 scopus 로고    scopus 로고
    • A novel family of channel-forming, autotransporting, bacterial virulence factors
    • Loveless, B. J., and M. H. Saier, Jr. 1997. A novel family of channel-forming, autotransporting, bacterial virulence factors. Mol. Membr. Biol. 14:113-123.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 113-123
    • Loveless, B.J.1    Saier Jr., M.H.2
  • 33
    • 0027494612 scopus 로고
    • Isogenic P-fimbrial deletion mutants of pyelonephritogenic Escherichia coli: The role of alpha Gal(1-4) beta Gal binding in virulence of a wild-type strain
    • Mobley, H. L., K. G. Jarvis, J. P. Elwood, D. I. Whittle, C. V. Lockatell, R. G. Russell, D. E. Johnson, M. S. Donnenberg, and J. W. Warren. 1993. Isogenic P-fimbrial deletion mutants of pyelonephritogenic Escherichia coli: the role of alpha Gal(1-4) beta Gal binding in virulence of a wild-type strain. Mol. Microbiol. 10:143-155.
    • (1993) Mol. Microbiol. , vol.10 , pp. 143-155
    • Mobley, H.L.1    Jarvis, K.G.2    Elwood, J.P.3    Whittle, D.I.4    Lockatell, C.V.5    Russell, R.G.6    Johnson, D.E.7    Donnenberg, M.S.8    Warren, J.W.9
  • 34
    • 0035145396 scopus 로고    scopus 로고
    • Plasmid-encoded toxin of enteroaggregative Escherichia coli is internalized by epithelial cells
    • Navarro-Garcia, F., A. Canizalez-Roman, J. Luna, C. Sears, and J. P. Nataro. 2001. Plasmid-encoded toxin of enteroaggregative Escherichia coli is internalized by epithelial cells. Infect. Immun. 69:1053-1060.
    • (2001) Infect. Immun. , vol.69 , pp. 1053-1060
    • Navarro-Garcia, F.1    Canizalez-Roman, A.2    Luna, J.3    Sears, C.4    Nataro, J.P.5
  • 35
    • 2542576380 scopus 로고    scopus 로고
    • The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli
    • Navarro-Garcia, F., A. Canizalez-Roman, B. Q. Sui, J. P. Nataro, and Y. Azamar. 2004. The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli. Infect. Immun. 72:3609-3621.
    • (2004) Infect. Immun. , vol.72 , pp. 3609-3621
    • Navarro-Garcia, F.1    Canizalez-Roman, A.2    Sui, B.Q.3    Nataro, J.P.4    Azamar, Y.5
  • 36
    • 0032948817 scopus 로고    scopus 로고
    • Cytoskeletal effects induced by Pet, the serine protease enterotoxin of enteroaggregative Escherichia coli
    • Navarro-Garcia, F., C. Sears, C. Eslava, A. Cravioto, and J. P. Nataro. 1999. Cytoskeletal effects induced by Pet, the serine protease enterotoxin of enteroaggregative Escherichia coli. Infect. Immun. 67:2184-2192.
    • (1999) Infect. Immun. , vol.67 , pp. 2184-2192
    • Navarro-Garcia, F.1    Sears, C.2    Eslava, C.3    Cravioto, A.4    Nataro, J.P.5
  • 39
    • 1342281315 scopus 로고    scopus 로고
    • Identification and molecular characterization of EatA, an autotransporter protein of enterotoxigenic Escherichia coli
    • Patel, S. K., J. Dotson, K. P. Allen, and J. M. Fleckenstein. 2004. Identification and molecular characterization of EatA, an autotransporter protein of enterotoxigenic Escherichia coli. Infect. Immun. 72:1786-1794.
    • (2004) Infect. Immun. , vol.72 , pp. 1786-1794
    • Patel, S.K.1    Dotson, J.2    Allen, K.P.3    Fleckenstein, J.M.4
  • 40
    • 0028348785 scopus 로고
    • Isolation and characterization of a gene involved in hemagglutination by an avian pathogenic Escherichia coli strain
    • Provence, D. L., and R. Curtiss III. 1994. Isolation and characterization of a gene involved in hemagglutination by an avian pathogenic Escherichia coli strain. Infect. Immun. 62:1369-1380.
    • (1994) Infect. Immun. , vol.62 , pp. 1369-1380
    • Provence, D.L.1    Curtiss III, R.2
  • 41
    • 0030817859 scopus 로고    scopus 로고
    • Use of a novel approach, termed island probing, identifies the Shigella flexneri she pathogenicity island which encodes a homolog of the immunoglobulin A protease-like family of proteins
    • Rajakumar, K., C. Sasakawa, and B. Adler. 1997. Use of a novel approach, termed island probing, identifies the Shigella flexneri she pathogenicity island which encodes a homolog of the immunoglobulin A protease-like family of proteins. Infect. Immun. 65:4606-4614.
    • (1997) Infect. Immun. , vol.65 , pp. 4606-4614
    • Rajakumar, K.1    Sasakawa, C.2    Adler, B.3
  • 46
    • 0029961503 scopus 로고    scopus 로고
    • Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins
    • Stein, M., B. Kenny, M. A. Stein, and B. B. Finlay. 1996. Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins. J. Bacteriol. 178:6546-6554.
    • (1996) J. Bacteriol. , vol.178 , pp. 6546-6554
    • Stein, M.1    Kenny, B.2    Stein, M.A.3    Finlay, B.B.4
  • 47
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi, D. G., and S. J. Hultgren. 2000. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12:420-430.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 48
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1992. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Bio/Technology 24:145-149.
    • (1992) Bio/Technology , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 49
    • 0009482260 scopus 로고
    • Reprinted from
    • [Reprinted from Proc. Natl. Acad. Sci. USA 76:4350-4354, 1979.]
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
  • 50
    • 0036565670 scopus 로고    scopus 로고
    • Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains
    • Veiga, E., E. Sugawara, H. Nikaido, V. de Lorenzo, and L. A. Fernandez. 2002. Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. EMBO J. 21:2122-2131.
    • (2002) EMBO J. , vol.21 , pp. 2122-2131
    • Veiga, E.1    Sugawara, E.2    Nikaido, H.3    De Lorenzo, V.4    Fernandez, L.A.5
  • 51
    • 0030042322 scopus 로고    scopus 로고
    • Spectrin: On the path from structure to function
    • Viel, A., and D. Branton. 1996. Spectrin: on the path from structure to function. Curr. Opin. Cell Biol. 8:49-55.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 49-55
    • Viel, A.1    Branton, D.2
  • 54
    • 0019792611 scopus 로고
    • Haemolysin contributes to virulence of extra-intestinal E. coli infections
    • Welch, R. A., E. P. Dellinger, B. Minshew, and S. Falkow. 1981. Haemolysin contributes to virulence of extra-intestinal E. coli infections. Nature 294:665-667.
    • (1981) Nature , vol.294 , pp. 665-667
    • Welch, R.A.1    Dellinger, E.P.2    Minshew, B.3    Falkow, S.4
  • 55
    • 0017164282 scopus 로고
    • Tables for the preparation of ammonium sulfate solutions
    • Wood, W. I. 1976. Tables for the preparation of ammonium sulfate solutions. Anal. Biochem. 73:250-257.
    • (1976) Anal. Biochem. , vol.73 , pp. 250-257
    • Wood, W.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.